In this study, an extracellular protease, but no chitinolytic enzyme-producing strain, Brevibacillus parabrevis TKU046, has been isolated and analyzed for the deproteinization testing of shrimp waste by liquid fermentation. Deproteinization assays of shrimp waste with this microbe showed 95% protein removal after 4 days fermentation. The efficiency of chitin extraction by B. parabrevis TKU046 on wastes of three shrimp species were also investigated in which the highest deproteinization was found on cooked tiger shrimp shell. Infrared spectra (IR) of the obtained chitin displayed characteristic profiles for chitin. The culture supernatant released after fermentation greatly exhibited growth enhancing effect on Lactobacillus rhamnosus. In addition, B. parabrevis TKU046 protease was isolated and determined the characteristics. The molecular mass of B. parabrevis TKU046 protease was determined as 32 kDa and 34 kDa, respectively, by SDS-PAGE and HPLC. Overall, the findings provide strong support for the potential candidacy of this enzyme as an effective and eco-friendly alternative to the conventional chemicals used for the deproteinization of shrimp heads in the chitin processing industry, as well as the production of prebiotics to be used in the nutraceutical industry.
Relation:
International Journal of Biological Macromolecules 131, p.706-715
